GSIC_ECOL6
ID GSIC_ECOL6 Reviewed; 306 AA.
AC Q8FJK9;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Glutathione transport system permease protein GsiC {ECO:0000250|UniProtKB:P75798};
GN Name=gsiC {ECO:0000250|UniProtKB:P75798}; OrderedLocusNames=c0916;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC -!- FUNCTION: Part of the ABC transporter complex GsiABCD involved in
CC glutathione import. Probably responsible for the translocation of the
CC substrate across the membrane. {ECO:0000250|UniProtKB:P75798}.
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (GsiA),
CC two transmembrane proteins (GsiC and GsiD) and a solute-binding protein
CC (GsiB). {ECO:0000250|UniProtKB:P75798}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:P75798}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. {ECO:0000305}.
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DR EMBL; AE014075; AAN79389.1; -; Genomic_DNA.
DR RefSeq; WP_000936053.1; NC_004431.1.
DR AlphaFoldDB; Q8FJK9; -.
DR SMR; Q8FJK9; -.
DR STRING; 199310.c0916; -.
DR EnsemblBacteria; AAN79389; AAN79389; c0916.
DR KEGG; ecc:c0916; -.
DR eggNOG; COG0601; Bacteria.
DR HOGENOM; CLU_036879_0_0_6; -.
DR OMA; MQEDYMR; -.
DR BioCyc; ECOL199310:C0916-MON; -.
DR Proteomes; UP000001410; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR CDD; cd06261; TM_PBP2; 1.
DR Gene3D; 1.10.3720.10; -; 1.
DR InterPro; IPR045621; BPD_transp_1_N.
DR InterPro; IPR000515; MetI-like.
DR InterPro; IPR035906; MetI-like_sf.
DR Pfam; PF00528; BPD_transp_1; 1.
DR Pfam; PF19300; BPD_transp_1_N; 1.
DR SUPFAM; SSF161098; SSF161098; 1.
DR PROSITE; PS50928; ABC_TM1; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..306
FT /note="Glutathione transport system permease protein GsiC"
FT /id="PRO_0000279991"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 30..102
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 124..134
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 135..155
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 156..168
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 190..228
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 250..277
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 299..306
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 95..292
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ SEQUENCE 306 AA; 34032 MW; 52DC82A3D6EB2406 CRC64;
MLNYVIKRLL GLIPTLFIVS VLVFLFVHML PGDPARLIAG PEADAQVIEL VRQQLGLDQP
LYHQFWHYIS NAVQGDLGLS MVSRRPVADE IASRFMPTLW LTITSMVWAV IFGMAAGIIA
AVWRNRWPDR LSMTIAVSGI SFPAFALGML LIQVFSVELG WLPTVGADSW QHYILPSLTL
GAAVAAVMAR FTRASFVDVL SEDYMRTARA KGVSETWVVL KHGLRNAMIP VVTMMGLQFG
FLLGGSIVVE KVFNWPGLGR LLVDSVEMRD YPVIQAEILL FSLEFILINL VVDVLYAAIN
PAIRYK